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PDBsum entry 1xnh

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Ligase PDB id
1xnh

 

 

 

 

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Contents
Protein chain
251 a.a. *
Waters ×37
* Residue conservation analysis
PDB id:
1xnh
Name: Ligase
Title: Crystal structure of nh3-dependent NAD+ synthetase from helicobacter pylori
Structure: Nh(3)-dependent NAD(+) synthetase. Chain: a. Engineered: yes
Source: Helicobacter pylori. Organism_taxid: 210. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.30Å     R-factor:   0.255     R-free:   0.295
Authors: G.B.Kang,Y.S.Kim,Y.J.Im,S.H.Rho,J.H.Lee,S.H.Eom
Key ref:
G.B.Kang et al. (2005). Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori. Proteins, 58, 985-988. PubMed id: 15645437 DOI: 10.1002/prot.20377
Date:
05-Oct-04     Release date:   05-Apr-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O25096  (NADE_HELPY) -  NH(3)-dependent NAD(+) synthetase from Helicobacter pylori (strain ATCC 700392 / 26695)
Seq:
Struc:
260 a.a.
251 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.1.5  - NAD(+) synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: deamido-NAD+ + NH4+ + ATP = AMP + diphosphate + NAD+ + H+
deamido-NAD(+)
+ NH4(+)
+ ATP
= AMP
+ diphosphate
+ NAD(+)
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1002/prot.20377 Proteins 58:985-988 (2005)
PubMed id: 15645437  
 
 
Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori.
G.B.Kang, Y.S.Kim, Y.J.Im, S.H.Rho, J.H.Lee, S.H.Eom.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Structure of H. pylori NAD^+ synthetase. (A) Stereo view of a ribbon diagram showing the dimeric structure of NAD^+ synthetase. The -helices are labeled A- L, and the -strands are labeled A- D. The two subunits are colored green and blue. The bound NaAD and ATP molecules are shown as the ball-and-stick models. The red line indicates a flexible loop region (residued 179-191). (B) Stereo view of the ATP binding site. Residues of the P-loop are colored cyan. (C) Stereo view of the NaAD binding site.
Figure 2.
Figure 2. The multiple sequence alignment of H. pylori, B. subtilis, and human NAD^+ synthetases. Sequences were aligned using ClustalX. Highly conserved residues are shaded in black and gray. The secondary structure elements of NAD^+ synthetase are indicated by arrows ( -strands), bars ( -helices), and lines (connecting loop). Residues constituting ATP and NaAD binding sites are indicated by open and filled circles, respectively.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 58, 985-988) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20857400 J.Bi, H.Wang, and J.Xie (2011).
Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets.
  J Cell Physiol, 226, 331-340.  
17642516 H.M.McDonald, P.S.Pruett, C.Deivanayagam, I.I.Protasevich, W.M.Carson, L.J.DeLucas, W.J.Brouillette, and C.G.Brouillette (2007).
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis.
  Acta Crystallogr D Biol Crystallogr, 63, 891-905.
PDB codes: 2pz8 2pza 2pzb
16783377 J.A.Khan, X.Tao, and L.Tong (2006).
Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents.
  Nat Struct Mol Biol, 13, 582-588.
PDB codes: 2gvg 2gvj 2gvl
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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